Co-operative binding interactions in affinity chromatography: Theoretical considerations

✍ Scribed by John Hubble

• Publisher: John Wiley and Sons
• Year: 1987
• Tongue: English
• Weight: 541 KB
• Volume: 30
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260300210

✦ Synopsis

A theoretical relationship has been developed to allow the effect of free ligand concentration on the capacity of an affinity chromatography matrix to be determined where the protein adsorbed shows co-operative binding. Computer simulations using literature values for association constants show that under optimal conditions resin capacity can be increased significantly in the presence of a small but finite concentration of free ligand. The model also allows prediction of the soluble ligand concentration required for biospecific elution. The results obtained suggest the possibility of a new elution technique, "reverse biospecific elution," that reduces the amount of free ligand required to effect elution.